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PKD1L1 Membrane Protein Introduction

Introduction of PKD1L1

PKD1L1 is encoded by PKD1L1 gene in human. The full-length cDNA sequence of PKD1L1, determined from human testis cDNA, encodes a 2849-amino-acid protein. The encoded protein is a member of polycystin polycystic kidney disease protein family. It contains two immunoglobulin (Ig)-like polycystic kidney disease (PKD) domains in the N-terminal extracellular region, a GPS motif, a small receptor for egg jelly (REJ) domain, 11 transmembrane segments, a polycystin-1, lipoxygenase, alpha-toxin (PLAT) domain, and a C-terminal intracellular coiled-coil (CC). Some studies have shown that this protein may be involved in the male reproductive system.

Basic Information of PKD1L1
Protein Name Polycystic kidney disease protein 1-like 1
Gene Name PKD1L1
Aliases PC1-like 1 protein, Polycystin-1L1
Organism Homo sapiens (Human)
UniProt ID Q8TDX9
Transmembrane Times 11
Length (aa) 2849
Sequence MAEEAAQNISDDQERCLQAACCLSFGGELSVSTDKSWGLHLCSCSPPGGGLWVEVYANHVLLMSDGKCGCPWCALNGKAEDRESQSPSSSASRQKNIWKTTSEAALSVVNEKTQAVVNEKTQAPLDCDNSADRIPHKPFIIIARAWSSGGPRFHHRRLCATGTADSTFSALLQLQGTTSAAAPCSLKMEASCCVLRLLCCAEDVATGLLPGTVTMETPTKVARPTQTSSQRVPLWPISHFPTSPRSSHGLPPGIPRTPSFTASQSGSEILYPPTQHPPVAILARNSDNFMNPVLNCSLEVEARAPPNLGFRVHMASGEALCLMMDFGDSSGVEMRLHNMSEAMAVTAYHQYSKGIFFHLLHFQLDMSTYKEAETQNTTLNVYLCQSENSCLEDSDPSNLGYELISAFVTKGVYMLKAVIYNEFHGTEVELGPYYVEIGHEAVSAFMNSSSVHEDEVLVFADSQVNQKSTVVIHHFPSIPSYNVSFISQTQVGDSQAWHSMTVWYKMQSVSVYTNGTVFATDTDITFTAVTKETIPLEFEWYFGEDPPVRTTSRSIKKRLSIPQWYRVMVKASNRMSSVVSEPHVIRVQKKIVANRLTSPSSALVNASVAFECWINFGTDVAYLWDFGDGTVSLGSSSSSHVYSREGEFTVEVLAFNNVSASTLRQQLFIVCEPCQPPLVKNMGPGKVQIWRSQPVRLGVTFEAAVFCDISQGLSYTWNLMDSEGLPVSLPAAVDTHRQTLILPSHTLEYGNYTALAKVQIEGSVVYSNYCVGLEVRAQAPVSVISEGTHLFFSRTTSSPIVLRGTQSFDPDDPGATLRYHWECATAGSPAHPCFDSSTAHQLDAAAPTVSFEAQWLSDSYDQFLVMLRVSSGGRNSSETRVFLSPYPDSAFRFVHISWVSFKDTFVNWNDELSLQAMCEDCSEIPNLSYSWDLFLVNATEKNRIEVPFCRVVGLLGSLGLGAISESSQLNLLPTEPGTADPDATTTPFSREPSPVTLGQPATSAPRGTPTEPMTGVYWIPPAGDSAVLGEAPEEGSLDLEPGPQSKGSLMTGRSERSQPTHSPDPHLSDFEAYYSDIQEAIPSGGRQPAKDTSFPGSGPSLSAEESPGDGDNLVDPSLSAGRAEPVLMIDWPKALLGRAVFQGYSSSGITEQTVTIKPYSLSSGETYVLQVSVASKHGLLGKAQLYLTVNPAPRDMACQVQPHHGLEAHTVFSVFCMSGKPDFHYEFSYQIGNTSKHTLYHGRDTQYYFVLPAGEHLDNYKVMVSTEITDGKGSKVQPCTVVVTVLPRYHGNDCLGEDLYNSSLKNLSTLQLMGSYTEIRNYITVITRILSRLSKEDKTASCNQWSRIQDALISSVCRLAFVDQEEMIGSVLMLRDLVSFSNKLGFMSAVLILKYTRALLAQGQFSGPFVIDKGVRLELIGLISRVWEVSEQENSKEEVYRHEEGITVISDLLLGCLSLNHVSTGQMEFRTLLHYNLQSSVQSLGSVQVHLPGDLAGHSPAGAETQSPCYISQLILFKKNPYPGSQAPGQIGGVVGLNLYTCSSRRPINRQWLRKPVMVEFGEEDGLDNRRNKTTFVLLRDKVNLHQFTELSENPQESLQIEIEFSKPVTRAFPVMLLVRFSEKPTPSDFLVKQIYFWDESIVQIYIPAASQKDASVGYLSLLDADYDRKPPNRYLAKAVNYTVHFQWIRCLFWDKREWKSERFSPQPGTSPEKVNCSYHRLAAFALLRRKLKASFEVSDISKLQSHPENLLPSIFIMGSVILYGFLVAKSRQVDHHEKKKAGYIFLQEASLPGHQLYAVVIDTGFRAPARLTSKVYIVLCGDNGLSETKELSCPEKPLFERNSRHTFILSAPAQLGLLRKIRLWHDSRGPSPGWFISHVMVKELHTGQGWFFPAQCWLSAGRHDGRVERELTCLQGGLGFRKLFYCKFTEYLEDFHVWLSVYSRPSSSRYLHTPRLTVSFSLLCVYACLTALVAAGGQEQPHLDVSPTLGSFRVGLLCTLLASPGAQLLSLLFRLSKEAPGSARVEPHSPLRGGAQTEAPHGPNSWGRIPDAQEPRKQPASAILSGSGRAQRKAASDNGTACPAPKLQVHGADHSRTSLMGKSHCCPPHTQAPSSGLEGLMPQWSRALQPWWSSAVWAICGTASLACSLGTGFLAYRFGQEQCVQWLHLLSLSVVCCIFITQPLMVCLMALGFAWKRRADNHFFTESLCEATRDLDSELAERSWTRLPFSSSCSIPDCAGEVEKVLAARQQARHLRWAHPPSKAQLRGTRQRMRRESRTRAALRDISMDILMLLLLLCVIYGRFSQDEYSLNQAIRKEFTRNARNCLGGLRNIADWWDWSLTTLLDGLYPGGTPSARVPGAQPGALGGKCYLIGSSVIRQLKVFPRHLCKPPRPFSALIEDSIPTCSPEVGGPENPYLIDPENQNVTLNGPGGCGTREDCVLSLGRTRTEAHTALSRLRASMWIDRSTRAVSVHFTLYNPPTQLFTSVSLRVEILPTGSLVPSSLVESFSIFRSDSALQYHLMLPQLVFLALSLIHLCVQLYRMMDKGVLSYWRKPRNWLELSVVGVSLTYYAVSGHLVTLAGDVTNQFHRGLCRAFMDLTLMASWNQRARWLRGILLFLFTLKCVYLPGIQNTMASCSSMMRHSLPSIFVAGLVGALMLAALSHLHRFLLSMWVLPPGTFTDAFPGLLFHFPRRSQKDCLLGLSKSDQRAMACYFGILLIVSATLCFGMLRGFLMTLPQKRKSFQSKSFVRLKDVTAYMWEKVLTFLRLETPKLEEAEMVENHNYYLDEFANLLDELLMKINGLSDSLQLPLLEKTSNNTGEARTEESPLVDISSYQAAEPADIKDF

Function of PKD1L1 Membrane Protein

PKD1L1 is a component of ciliary calcium channel that regulates calcium concentration within primary cilia without affecting cytoplasmic calcium concentration. A study has shown that PKD1L1 can interact and interdependently colocalize with PKD2 at the cilia in Kupffer's vesicle (KV, an organ equivalent to the node), functioning as the nodal flow sensor in the motile cilia. The loss of PKD1L1 function is known to cause laterality defects in mouse and medaka fish models. Furthermore, PKD1L1 has been shown to be expressed in testis and in the fetal and adult heart. The most abundant and specific expression of PKD1L1 is found in Leydig cells, a known source of testosterone production, in mouse testis. These data suggest that PKD1L1 may play a role in the heart and in the male reproductive system.

Schematic representation of the human PKD1L1 structural domains. Fig.1 Schematic representation of the human PKD1L1 structural domains. (Vetrini, 2016)

Application of PKD1L1 Membrane Protein in Literature

  1. Vetrini F., et al. Bi-allelic mutations in PKD1L1 are associated with laterality defects in humans. Am J Hum Genet. 2016, 99(4):886-893. PubMed ID: 27616478

    This article identifies two homozygous mutations in PKD1L1 in three individuals who presented with laterality defects. These data expand the information of genetic heterogeneity of laterality defects in humans.

  2. Kamura K., et al. Pkd1l1 complexes with Pkd2 on motile cilia and functions to establish the left-right axis. Development. 2011, 138(6):1121-9. PubMed ID: 21307098

    In this paper, a new model of ciliary action in left-right patterning is proposed, in which KV cilia has a dual role: to generate nodal flow and to interpret it through Pkd1L1-Pkd2 complexes.

  3. Field S., et al. Pkd1l1 establishes left-right asymmetry and physically interacts with Pkd2. Development. 2011, 138(6):1131-1142. PubMed ID: 21307093

    This study shows that Pkd1L1 is the elusive Pkd2 binding partner required for L-R patterning and support the two-cilia hypothesis.

  4. Yuasa T., et al. The sequence, expression, and chromosomal localization of a novel polycystic kidney disease 1-like gene, PKD1L1, in human. Genomics. 2002, 79(3):0-386. PubMed ID: 11863367

    This article suggests that PKD1L1 may exert a role in the heart and in the male reproductive system.

PKD1L1 Preparation Options

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Reference

  1. Vetrini F, et al. (2016). Bi-allelic mutations in PKD1L1 are associated with laterality defects in humans. Am J Hum Genet. 99(4): 886-893.

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